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Our bodies are filled with proteins; complex molecules that drive nearly all processes within a cell. Some proteins have a stable, folded structure, while others are flexible and intrinsically disordered. This research contributes to our understanding of both types of proteins.

A key part of the study focused on the cytoskeleton: the cell’s internal framework that determines shape, movement, and transport. Within this system, microtubules, tube-like protein structures, play a central role. We investigated enzymes that chemically modify microtubules and discovered, among other findings, a new enzyme called MATCAP, which appears to be important for brain cell development.

In addition, a comprehensive analysis was carried out on so-called intrinsically disordered protein regions: flexible parts of proteins that lack a fixed structure. Using a large dataset (CHAOS), we found that the majority of human proteins contain such regions, often located at the ends of proteins, and that these are enriched in chemical modifications.

These findings offer new insights into how cells function. They also provide valuable leads for the development of new drugs, for instance targeting the cytoskeleton or disordered protein regions, which could be relevant for treating diseases such as cancer or neurological disorders.